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Protein

Envelope glycoprotein B

Gene

gB

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moities of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.UniRule annotation

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein BUniRule annotation
Short name:
gBUniRule annotation
Gene namesi
Name:gBUniRule annotation
ORF Names:BALF4
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host endosome membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host Golgi apparatus membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation

  • Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 732Virion surfaceUniRule annotationAdd BLAST711
Transmembranei733 – 753HelicalUniRule annotationAdd BLAST21
Topological domaini754 – 857IntravirionUniRule annotationAdd BLAST104

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host Golgi apparatus, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112 – 113WY → HR: Loss of fusion with epithelial cells. 1 Publication2
Mutagenesisi193 – 196WLIW → RVEA: Loss of fusion with epithelial cells. 1 Publication4
Mutagenesisi428 – 432RRRRR → DDDDK: Complete loss of proteolytic cleavage. 1 Publication5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21UniRule annotationAdd BLAST21
ChainiPRO_000003819022 – 857Envelope glycoprotein BUniRule annotationAdd BLAST836

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 528UniRule annotationCombined sources1 Publication
Disulfide bondi68 ↔ 484UniRule annotationCombined sources1 Publication
Glycosylationi76N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi141 ↔ 206UniRule annotationCombined sources1 Publication
Glycosylationi163N-linked (GlcNAc...); by hostUniRule annotation1 Publication1
Glycosylationi290N-linked (GlcNAc...); by hostUniRule annotation1 Publication1
Disulfide bondi295 ↔ 342UniRule annotationCombined sources1 Publication
Glycosylationi329N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi348N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi395N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi436N-linked (GlcNAc...); by hostUniRule annotation1
Disulfide bondi551 ↔ 588UniRule annotation
Glycosylationi563N-linked (GlcNAc...); by hostUniRule annotation1
Glycosylationi629N-linked (GlcNAc...); by hostUniRule annotation1 Publication1

Post-translational modificationi

A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei432 – 433Cleavage; by host furinSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked. Binds to heparan sulfate proteoglycans. Interacts with gH/gL heterodimer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-47669N.
IntActiP03188. 10 interactors.
MINTiMINT-6768112.

Structurei

Secondary structure

1857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi58 – 60Combined sources3
Beta strandi77 – 87Combined sources11
Beta strandi92 – 110Combined sources19
Beta strandi115 – 125Combined sources11
Helixi129 – 135Combined sources7
Turni136 – 138Combined sources3
Beta strandi140 – 149Combined sources10
Beta strandi152 – 157Combined sources6
Helixi158 – 160Combined sources3
Beta strandi165 – 167Combined sources3
Beta strandi179 – 183Combined sources5
Beta strandi197 – 215Combined sources19
Beta strandi222 – 224Combined sources3
Beta strandi229 – 232Combined sources4
Turni248 – 250Combined sources3
Beta strandi251 – 257Combined sources7
Helixi262 – 264Combined sources3
Beta strandi272 – 278Combined sources7
Beta strandi283 – 287Combined sources5
Helixi291 – 293Combined sources3
Beta strandi296 – 310Combined sources15
Beta strandi315 – 319Combined sources5
Turni320 – 323Combined sources4
Beta strandi324 – 329Combined sources6
Helixi341 – 343Combined sources3
Helixi344 – 356Combined sources13
Turni357 – 361Combined sources5
Beta strandi362 – 368Combined sources7
Beta strandi370 – 374Combined sources5
Beta strandi379 – 387Combined sources9
Helixi458 – 498Combined sources41
Helixi502 – 510Combined sources9
Beta strandi516 – 519Combined sources4
Beta strandi522 – 525Combined sources4
Beta strandi533 – 538Combined sources6
Beta strandi556 – 560Combined sources5
Beta strandi567 – 572Combined sources6
Beta strandi576 – 579Combined sources4
Beta strandi593 – 598Combined sources6
Beta strandi601 – 606Combined sources6
Beta strandi609 – 615Combined sources7
Turni616 – 618Combined sources3
Helixi646 – 650Combined sources5
Helixi657 – 673Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortaliP03188.
SMRiP03188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03188.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 114Involved in fusion and/or binding to host membraneUniRule annotation7
Regioni192 – 200Involved in fusion and/or binding to host membraneUniRule annotation9
Regioni561 – 620OligomerizationAdd BLAST60
Regioni678 – 730Hydrophobic membrane proximal regionUniRule annotationAdd BLAST53
Regioni709 – 729Hydrophobic membrane proximal regionAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi428 – 432Poly-Arg5
Compositional biasi836 – 839Poly-Arg4

Sequence similaritiesi

Belongs to the herpesviridae glycoprotein B family.UniRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19255.

Family and domain databases

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03188-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV
60 70 80 90 100
CELSSHGDLF RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT
110 120 130 140 150
KIVTNILIYN GWYADSVTNR HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD
160 170 180 190 200
GLTRVYVDRD GVNITVNLKP TGGLANGVRR YASQTELYDA PGWLIWTYRT
210 220 230 240 250
RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN KETFHERADS
260 270 280 290 300
FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW
310 320 330 340 350
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT
360 370 380 390 400
MHEKYEAVQD RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT
410 420 430 440 450
TPTSSPPSSP SPPAPSAARG STPAAVLRRR RRDAGNATTP VPPTAPGKSL
460 470 480 490 500
GTLNNPATVQ IQFAYDSLRR QINRMLGDLA RAWCLEQKRQ NMVLRELTKI
510 520 530 540 550
NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK SMRVPGSETM
560 570 580 590 600
CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN
610 620 630 640 650
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR
660 670 680 690 700
ASNVFDLEGI FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL
710 720 730 740 750
GSVGQSITNL VSTVGGLFSS LVSGFISFFK NPFGGMLILV LVAGVVILVI
760 770 780 790 800
SLTRRTRQMS QQPVQMLYPG IDELAQQHAS GEGPGINPIS KTELQAIMLA
810 820 830 840 850
LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY HDPETAAALL

GEAETEF
Length:857
Mass (Da):95,639
Last modified:July 21, 1986 - v1
Checksum:iD9BCE9487D8A1411
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1.
AJ507799 Genomic DNA. Translation: CAD53463.1.
PIRiA03749. QQBE1L.
RefSeqiYP_401713.1. NC_007605.1.

Genome annotation databases

GeneIDi3783680.
KEGGivg:3783680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24806.1.
AJ507799 Genomic DNA. Translation: CAD53463.1.
PIRiA03749. QQBE1L.
RefSeqiYP_401713.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FVCX-ray3.20A23-685[»]
ProteinModelPortaliP03188.
SMRiP03188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47669N.
IntActiP03188. 10 interactors.
MINTiMINT-6768112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783680.
KEGGivg:3783680.

Phylogenomic databases

KOiK19255.

Miscellaneous databases

EvolutionaryTraceiP03188.

Family and domain databases

HAMAPiMF_04032. HSV_GB. 1 hit.
InterProiIPR000234. Herpes_Glycoprot_B.
[Graphical view]
PfamiPF00606. Glycoprotein_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGB_EBVB9
AccessioniPrimary (citable) accession number: P03188
Secondary accession number(s): Q777B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.